5ND1

Viral evolution results in multiple, surface-allocated enzymatic activities in a fungal double-stranded RNA virus

5ND1 の概要

• エントリーDOI: 10.2210/pdb5nd1/pdb
• EMDBエントリー: 3619
• 分子名称: Capsid protein (2 entities in total)
• 機能のキーワード: rnqv1, dsrna virus, fungal virus, virus
• 由来する生物種: Rosellinia necatrix quadrivirus 1 (RnQV1); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 261221.72

構造登録者

Mata, C.P.,Luque, D.,Gomez Blanco, J.,Rodriguez, J.M.,Suzuki, N.,Ghabrial, S.A.,Carrascosa, J.L.,Trus, B.L.,Caston, J.R. (登録日: 2017-03-07, 公開日: 2017-11-29, 最終更新日: 2024-06-12)

主引用文献

Mata, C.P.,Luque, D.,Gomez-Blanco, J.,Rodriguez, J.M.,Gonzalez, J.M.,Suzuki, N.,Ghabrial, S.A.,Carrascosa, J.L.,Trus, B.L.,Caston, J.R.
Acquisition of functions on the outer capsid surface during evolution of double-stranded RNA fungal viruses.
PLoS Pathog., 13:e1006755-e1006755, 2017

PubMed Abstract: Unlike their counterparts in bacterial and higher eukaryotic hosts, most fungal viruses are transmitted intracellularly and lack an extracellular phase. Here we determined the cryo-EM structure at 3.7 Å resolution of Rosellinia necatrix quadrivirus 1 (RnQV1), a fungal double-stranded (ds)RNA virus. RnQV1, the type species of the family Quadriviridae, has a multipartite genome consisting of four monocistronic segments. Whereas most dsRNA virus capsids are based on dimers of a single protein, the ~450-Å-diameter, T = 1 RnQV1 capsid is built of P2 and P4 protein heterodimers, each with more than 1000 residues. Despite a lack of sequence similarity between the two proteins, they have a similar α-helical domain, the structural signature shared with the lineage of the dsRNA bluetongue virus-like viruses. Domain insertions in P2 and P4 preferential sites provide additional functions at the capsid outer surface, probably related to enzyme activity. The P2 insertion has a fold similar to that of gelsolin and profilin, two actin-binding proteins with a function in cytoskeleton metabolism, whereas the P4 insertion suggests protease activity involved in cleavage of the P2 383-residue C-terminal region, absent in the mature viral particle. Our results indicate that the intimate virus-fungus partnership has altered the capsid genome-protective and/or receptor-binding functions. Fungal virus evolution has tended to allocate enzyme activities to the virus capsid outer surface.

PubMed: 29220409
DOI: 10.1371/journal.ppat.1006755

実験手法

ELECTRON MICROSCOPY (3.7 Å)